Response to Copper Stress in Streptomyces lividans Extends beyond Genes under Direct Control of a Copper-sensitive Operon Repressor Protein (CsoR)

Dwarakanath, Srivatsa; Chaplin, Amanda K.; Hough, Michael A.; Rigali, Sébastien; Vijgenboom, Erik; Worrall, J.A.R.

doi:10.1074/jbc.m112.352740

Cited by 54 publications

(150 citation statements)

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“…We have recently developed a CsoR from Geobacillus thermodenitrificans (Gt) as a model system for this purpose (28). We show here that Gt CsoR is representative of CsoRs from other mesophilic bacilli, including B. subtilis (16) and the pathogenic bacteria L. monocytogenes (19) and Bacillus anthracis, and is more distantly related to other CsoRs characterized previously (14,18,20). The x-ray crystallographic structure of Cu(I)-bound Gt CsoR and companion NMR and small angle x-ray scattering (SAXS) experiments provide new insights into the Cu(I)-dependent conformational switching associated with allosteric negative regulation of DNA binding by Cu(I).…”

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confidence: 64%

“…6, A and B, and supplemental Movie S1). In fact, global superposition of our apoprotein scattering envelope on the structure of apo-S. lividans CsoR that lacks an N-terminal tail (20) gives a statistically better fit than when superimposed on our structure of Cu(I)-Gt CsoR (Fig. 10, A and C).…”

Section: Saxs Analysis Of Cu(i)-mediated Allosteric Switching-wementioning

confidence: 86%

“…The copper-sensitive operon repressor (CsoR) 2 was discovered in M. tuberculosis (14) as the first representative of the DUF156 family; other CsoRs were subsequently studied in Bacillus subtilis, Staphylococcus aureus, Thermus thermophilus, L. monocytogenes, and Streptomyces lividans (15)(16)(17)(18)(19)(20). A second M. tuberculosis CsoR paralog, RicR, was shown to be involved in the regulation of several genes only found in pathogenic mycobacteria in response to copper stress (2).…”

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confidence: 99%

“…The major structural unit of the dimer is an ␣1-␣2-␣1Ј-␣2Ј four-helix bundle, with the Cu(I) bound to an S 2 N trigonal planar coordination chelate at the periphery of the bundle; the C-terminal ␣3 helices mediate many dimer-dimer contacts within the tetramer. Two copper-free crystal structures subsequently reported for T. thermophilus and S. lividans CsoRs adopt the same dimer-of-dimers architecture (18,20). ApoCsoR binds specifically to its operator DNA in a 2:1 tetramer/ operator binding stoichiometry (16,26) but lacks a canonical DNA binding domain; as a result, precisely how CsoR interacts with its pseudo-2-fold symmetric DNA operator remains unclear.…”

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confidence: 99%

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Cu(I)-mediated Allosteric Switching in a Copper-sensing Operon Repressor (CsoR)

Chang

Coyne

Cubillas

et al. 2014

Journal of Biological Chemistry

139

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Copper is an essential transition metal for living organisms but it is detrimental in excess. The metalloregulatory protein copper‐sensing operon repressor (CsoR) in bacteria has evolved to prevent cytoplasmic copper toxicity. Cu(I)‐binding to tetrameric CsoRs mediates transcriptional derepression of copper resistance genes but the mechanism is unknown. A phylogenetic analysis of 227 DUF156 protein members including biochemically or structurally characterized CsoR/RcnR repressors reveals that Geobacillus thermodenitrificans (Gt) CsoR characterized here is representative of CsoRs from pathogenic bacilli Listeria monocytogenes and Bacillus anthracis. The 2.56 Å structure of Cu(I)‐bound Gt CsoR reveals that Cu(I) binding induces a kink in the α2‐helix between two conserved copper‐ligating residues and folds an N‐terminal tail (residues 12‐19) over the Cu(I) binding site. NMR studies of Gt CsoR reveal that this tail is flexible in the apo‐state with these dynamics quenched upon Cu(I) binding. Small angle X‐ray scattering (SAXS) experiments on an N‐terminally truncated Gt CsoR (∆2‐10) reveal that the Cu(I)‐bound tetramer is hydrodynamically more compact than is the apo‐state. A mutational analysis of residues critical to N‐terminal tail folding reveals that these residues function to stabilize the apoprotein‐DNA complex and/or control the extent of allosteric negative regulation of DNA binding by Cu(I), but to varying degrees. The mechanism of Cu(I)‐mediated allosteric switching in CsoRs is discussed. Grant Funding Source: Supported by NIH grant GM042569

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confidence: 64%

Section: Saxs Analysis Of Cu(i)-mediated Allosteric Switching-wementioning

confidence: 86%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Cu(I)-mediated Allosteric Switching in a Copper-sensing Operon Repressor (CsoR)

Chang

Coyne

Cubillas

et al. 2014

Journal of Biological Chemistry

139

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“…However, neither is CopA2, a second Cu efflux pump that is not required for Cu tolerance in P. aeruginosa, but is suggested to be involved in export coupled to Cu acquisition by cytochrome c oxidase (88). The S. lividans Csp3 is up-regulated by 0.4 mM Cu(II) and in a csoR (copper-sensitive operon repressor) deletion mutant (89). A transcriptomic study of the Gram negative bacterium Sphingobium sp.…”

Section: The Functions Of Cspsmentioning

confidence: 99%

Bacterial copper storage proteins

Dennison

David

Lee

2018

Journal of Biological Chemistry

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Metal Specificity of Metallosensors

Higgins

Giedroc

2004

Encyclopedia of Inorganic and Bioinorganic Chemistry

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Transition metal ions are biologically required yet toxic when in excess. As such, prokaryotes have developed metal homeostasis systems that allow for the acquisition of essential metal ions, the delivery of these metal ions to target proteins, and the export of metal ions from the cell. Specialized metal‐binding proteins termed metallosensors bind to a cognate metal ion(s) in the cell and either transcriptionally repress the expression of importers or de‐repress the expression of exporters or sequestration systems and therefore govern cellular metal homeostasis. Metallosensors must be selective and appropriately sensitive toward the binding of their cognate metals. Prokaryotic metallosensors have been identified in ten different protein structural families. Each family exploits either one general metal‐binding‐site region, individual members of which have evolved different coordination sites, or alternatively, employs multiple metal‐binding sites to effect coordination of different metal ions. There is now broad support for the hypothesis that metal responsiveness in metallosensors is most closely linked to the coordination number and geometry adopted by cognate metal ion(s), and this is the subject of this article. Since a range of metal ions can be collectively sensed by a single repressor family, a particular protein fold cannot be specific for one particular metal ion. In fact, the converse is true: nature has used convergent evolution to evolve metal‐specific sensors on a variety of structural scaffolds that exploit common principles of coordination chemistry (ligand type, coordination number, and geometry) to effect the same biological outcome.

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Response to Copper Stress in Streptomyces lividans Extends beyond Genes under Direct Control of a Copper-sensitive Operon Repressor Protein (CsoR)

Cited by 54 publications

References 53 publications

Cu(I)-mediated Allosteric Switching in a Copper-sensing Operon Repressor (CsoR)

Cu(I)-mediated Allosteric Switching in a Copper-sensing Operon Repressor (CsoR)

Bacterial copper storage proteins

Metal Specificity of Metallosensors

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